期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 289, 期 19, 页码 13374-13384出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M114.547448
关键词
Amino Acid Transport; Liposomes; Mitochondrial Transport; Recombinant Protein Expression; Reconstitution of Membrane Transporters; SLC25 Family; SLC25A29; Basic Amino Acids; Membrane Transport Protein; Mitochondrial Carrier
资金
- Ministero dell'Universita e della Ricerca (MIUR)
- National Research Council (CNR)
- Centro di Eccellenza in Genomica Comparata (CEGBA)
- Apulia Region
- Italian Human ProteomeNet Grant (MIUR) [RBRN07BMCT_009]
Background: SLC25A29 encoded by the human SLC25A29 gene was suggested to be a mitochondrial carnitine/acylcarnitine- or ornithine-like transporter. Results: The recombinant, purified SLC25A29 transports arginine, lysine, and to a lesser extent ornithine and histidine but not carnitine and acylcarnitines. Conclusion: SLC25A29 is a mitochondrial transporter for basic amino acids. Significance: Another member of the mitochondrial carrier superfamily responsible for 12 monogenic diseases has been thoroughly characterized. The human genome encodes 53 members of the solute carrier family 25 (SLC25), also called the mitochondrial carrier family, many of which have been shown to transport carboxylates, amino acids, nucleotides, and cofactors across the inner mitochondrial membrane, thereby connecting cytosolic and matrix functions. In this work, a member of this family, SLC25A29, previously reported to be a mitochondrial carnitine/acylcarnitine- or ornithine-like carrier, has been thoroughly characterized biochemically. The SLC25A29 gene was overexpressed in Escherichia coli, and the gene product was purified and reconstituted in phospholipid vesicles. Its transport properties and kinetic parameters demonstrate that SLC25A29 transports arginine, lysine, homoarginine, methylarginine and, to a much lesser extent, ornithine and histidine. Carnitine and acylcarnitines were not transported by SLC25A29. This carrier catalyzed substantial uniport besides a counter-exchange transport, exhibited a high transport affinity for arginine and lysine, and was saturable and inhibited by mercurial compounds and other inhibitors of mitochondrial carriers to various degrees. The main physiological role of SLC25A29 is to import basic amino acids into mitochondria for mitochondrial protein synthesis and amino acid degradation.
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